[Characteristics of the key enzyme regulation of peripheral p-xylene metabolism in Pseudomonas aeruginosa].
The regulation of p-xylene methylhydroxylase, metapyrocatechase, pyrocatechase and protocatechoate-3,4-dioxygenase was studied in Pseudomonas aeruginosa 2x. Methylhydroxylase, the first enzyme of p-xylene oxidation, was shown to be synthesized in the strain in a constitutive manner and to be regulated at the level of the enzyme activity. Metapyrocatechase, protocatechase and pyrocatechase are inducible enzymes; these are repressed to a different extent by the end products of p-xylene oxidation. Metapyrocatechase has a broader substrate specificity as compared to pyrocatechase and is induced by a greater number of substrates, the affinity for different substrates depending on the structure of an inductor. Presumably, two isofunctional metapyrocatechases exist in P. aeruginosa 2 x.
D050548:Catechol 1,2-Dioxygenase; D050557:Catechol 2,3-Dioxygenase; D049308:Dioxygenases; D004305:Dose-Response Relationship, Drug; D004790:Enzyme Induction / Q000187:drug effects; D006899:Mixed Function Oxygenases / Q000096:biosynthesis*; D010084:Oxidation-Reduction / Q000187:drug effects; D010105:Oxygenases / Q000096:biosynthesis*; D011520:Protocatechuate-3,4-Dioxygenase / Q000096:biosynthesis*; D011550:Pseudomonas aeruginosa / Q000378:metabolism*; D014992:Xylenes / Q000378:metabolism*
D014992:Xylenes; D006899:Mixed Function Oxygenases; D010105:Oxygenases; D049308:Dioxygenases; D050548:Catechol 1,2-Dioxygenase; D050557:Catechol 2,3-Dioxygenase; D011520:Protocatechuate-3,4-Dioxygenase; C026267:4-xylene methylhydroxylase
Osobennosti reguliatsii kliuchevykh fermentov periferiĭnogo metabolizma p-ksilola u Pseudomonas aeruginosa.